Decolorization of azo and anthraquinone dyes by crude laccase produced by Lentinus crinitus in solid state cultivation

Othman AM, Elsayed MA, Elshafei AM, Hassan MM (2018) Purification and biochemical characterization of two isolated laccase isoforms from Agaricus bisporus CU13 and their potency in dye decolorization. Int J Biol Macromol 113:1142–1148. https://doi.org/10.1016/j.ijbiomac.2018.03.043

Vikrant K, Giri BS, Raza N, Roy K, Kim K-H, Rai BN, Singh RS (2018) Recent advancements in bioremediation of dye: current status and challenges. Bioresour Technol 253:355–367. https://doi.org/10.1016/j.biortech.2018.01.029

Leite LDS, Maselli BDS, Umbuzeiro GDA, Nogueira RFP (2016) Monitoring ecotoxicity of disperse red 1 dye during photo-Fenton degradation. Chemosphere 148:511–517. https://doi.org/10.1016/j.chemosphere.2016.01.053

Xiang X, Chen X, Dai R, Luo Y, Ma P, Ni S, Ma C (2016) Anaerobic digestion of recalcitrant textile dyeing sludge with alternative pretreatment strategies. Bioresour Technol 222:252–260. https://doi.org/10.1016/j.biortech.2016.09.098

Ali H (2010) Biodegradation of synthetic dyes - a review. Water Air Soil Pollut 213:251–273. https://doi.org/10.1007/s11270-010-0382-4

Rawat D, Mishra V, Sharma RS (2016) Detoxification of azo dyes in the context of environmental processes. Chemosphere 155:591–605. https://doi.org/10.1016/j.chemosphere.2016.04.068

Forootanfar H, Rezaei S, Zeinvand-Lorestani H, Tahmasbi H, Mogharabi M, Ameri A, Faramarzi MA (2016) Studies on the laccase-mediated decolorization, kinetic, and microtoxicity of some synthetic azo dyes. J Environ Health Sci Eng 14:7–9. https://doi.org/10.1186/s40201-016-0248-9

Joo DJ, Shin WS, Choi J-H et al (2007) Decolorization of reactive dyes using inorganic coagulants and synthetic polymer. Dyes Pigments 73:59–64. https://doi.org/10.1016/j.dyepig.2005.10.011

Perlatti B, da Silva MFG, Fernandes JB, Forim MR (2012) Validation and application of HPLC–ESI-MS/MS method for the quantification of RBBR decolorization, a model for highly toxic molecules, using several fungi strains. Bioresour Technol 124:37–44. https://doi.org/10.1016/j.biortech.2012.08.032

Kaushik P, Malik A (2009) Fungal dye decolourization: recent advances and future potential. Environ Int 35:127–141. https://doi.org/10.1016/j.envint.2008.05.010

Rodríguez-Couto S (2011) Production of laccase and decolouration of the textile dye Remazol brilliant blue R in temporary immersion bioreactors. J Hazard Mater 194:297–302. https://doi.org/10.1016/j.jhazmat.2011.07.098

Martínková L, Kotik M, Marková E, Homolka L (2016) Biodegradation of phenolic compounds by Basidiomycota and its phenol oxidases: a review. Chemosphere 149:373–382. https://doi.org/10.1016/j.chemosphere.2016.01.022

Maté DM, Alcalde M (2016) Laccase: a multi-purpose biocatalyst at the forefront of biotechnology. Microb Biotechnol 10:1457–1467. https://doi.org/10.1111/1751-7915.12422

Soccol CR, Costa ESFD, Letti LAJ, Karp SG, Woiciechowski AL, Vandenberghe LPDS (2017) Recent developments and innovations in solid state fermentation. Biotechnol Res Innov 1:52–71. https://doi.org/10.1016/j.biori.2017.01.002

Hernández C, Silva A-MFD, Ziarelli F, Perraud-Gaime I, Gutiérrez-Rivera B, García-Pérez JA, Alarcón E (2016) Laccase induction by synthetic dyes in Pycnoporus sanguineus and their possible use for sugar cane bagasse delignification. Appl Microbiol Biotechnol 101:1189–1201. https://doi.org/10.1007/s00253-016-7890-0

Karp SG, Faraco V, Amore A, Birolo L, Giangrande C, Soccol VT, Pandey A, Soccol CR (2012) Characterization of laccase isoforms produced by Pleurotus ostreatus in solid state fermentation of sugarcane bagasse. Bioresour Technol 114:735–739. https://doi.org/10.1016/j.biortech.2012.03.058

Madeira JV Jr, Contesini FJ, Calzado F, Rubio MV, Zubieta MP, Lopes DB, Melo RR (2017) Agro-industrial residues and microbial enzymes: an overview on the eco-friendly bioconversion into high value-added products. In: Brahmachari G, Demain AL, Adrio JL (eds) Biotechnology of microbial enzymes: production, biocatalysis and industrial applications. Elsevier/AP, Tokyo, pp 475–511

CONAB Companhia Nacional de Abastecimento (2018) Brazilian crop 2017/18. Available at http://www.conab.gov.br. Accessed 23 november 2018

Giardina P, Faraco V, Pezzella C, Piscitelli A, Vanhulle S, Sannia G (2009) Laccases: a never-ending story. Cell Mol Life S 67:369–385. https://doi.org/10.1007/s00018-009-0169-1

D'Agostini ÉC, Mantovani TRD, Valle JS, Paccola-Meirelles LD, Colauto NB, Linde GA (2011) Low carbon/nitrogen ratio increases laccase production from basidiomycetes in solid substrate cultivation. Sci Agric 68:295–300. https://doi.org/10.1590/s0103-90162011000300004

Marim RA, Oliveira ACC, Marquezoni R et al (2016) Use of sugarcane molasses by Pycnoporus sanguineus for the production of laccase for dye decolorization. Genet Mol Res 15. https://doi.org/10.4238/gmr15048972

Drechsler-Santos ER, Wartchow F, Coimbra VRM, Gibertoni TB, Cavalcanti MAQ (2012) Studies on lentinoid fungi (Lentinus and Panus) from the semi-arid region of Brazil. J Torrey Bot Soc 139:437–446. https://doi.org/10.3159/torrey-d-12-00019.1

Vargas-Isla R, Ishikawa NK (2008) Optimal conditions of in vitro mycelial growth of Lentinus strigosus, an edible mushroom isolated in the Brazilian Amazon. Mycoscience 49:215–219. https://doi.org/10.1007/s10267-007-0404-2

Umeo S, Souza G, Rapachi P, Garcia DM, Paccola-Meirelles LD, Valle JS, Colauto NB, Linde GA (2015) Screening of basidiomycetes in submerged cultivation based on antioxidant activity. Genet Mol Res 14:9907–9914. https://doi.org/10.4238/2015.august.19.25

Valle JS, Vandenberghe LPS, Santana TT, Almeida PH, Pereira AM, Linde GA, Colauto NB, Soccol CR (2014) Optimum conditions for inducing laccase production in Lentinus crinitus. Genet Mol Res 13:8544–8551. https://doi.org/10.4238/2014.october.20.31

Cambri G, Sousa MMLD, Fonseca DDM, Marchini FK, Silveira JLMD, Paba J (2016) Analysis of the biotechnological potential of a Lentinus crinitus isolate in the light of its secretome. J Proteome Res 15:4557–4568. https://doi.org/10.1021/acs.jproteome.6b00636

Marim RA, Avelino KV, Linde GA, Colauto NB, Valle JS (2018) Lentinus crinitus strains respond differently to cultivation pH and temperature. Genet Mol Res 17. https://doi.org/10.4238/gmr16039885

Almeida PH, Oliveira ACC, Souza GPN, Friedrich JC, Linde GA, Colauto NB, Valle JS (2018) Decolorization of Remazol brilliant blue R with laccase from Lentinus crinitus grown in agro-industrial by-products. Ann Braz Acad Sci 90:3463–3473. https://doi.org/10.1590/0001-3765201820170458

Niebisch CH, Malinowski AK, Schadeck R, Mitchell DA, Kava-Cordeiro V, Paba J (2010) Decolorization and biodegradation of reactive blue 220 textile dye by Lentinus crinitus extracellular extract. J Hazard Mater 180:316–322. https://doi.org/10.1016/j.jhazmat.2010.04.033

Valle JS, Vandenberghe LPDS, Santana TT, Linde GA, Colauto NB, Soccol CR (2014) Optimization of Agaricus blazei laccase production by submerged cultivation with sugarcane molasses. Afr J Microbiol Res 8:939–946. https://doi.org/10.5897/ajmr2013.6508

Kuwahara M, Glenn JK, Morgan MA, Gold MH (1984) Separation and characterization of two extracelluar H2O2-dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium. FEBS Lett 169:247–250. https://doi.org/10.1016/0014-5793(84)80327-0

Magalhães DB, Carvalho MEAD, Bon E, Neto JSA, Kling SH (1996) Colorimetric assay for lignin peroxidase activity determination using methylene blue as substrate. Biotechnol Tech 10:273–276. https://doi.org/10.1007/bf00184028

Conceição TA, Koblitz MGB, Kamida HM, Góes-Neto A (2017) Study of the production of Lentinus crinitus (L.) Fr. Lignolytic enzymes grown on agro-industrial waste. Adv Biosci Biotechnol 8:259–272. https://doi.org/10.4236/abb.2017.88019

Elisashvili V, Kachlishvili E (2009) Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes. J Biotechnol 144:37–42. https://doi.org/10.1016/j.jbiotec.2009.06.020

Silva CMMS, Melo ISD, Oliveira PRD (2005) Ligninolytic enzyme production by Ganoderma spp. Enzyme Microb Tech 37:324–329. https://doi.org/10.1016/j.enzmictec.2004.12.007

Martani F, Beltrametti F, Porro D, Branduardi P, Lotti M (2017) The importance of fermentative conditions for the biotechnological production of lignin modifying enzymes from white-rot fungi. FEMS Microbiol Lett 364. https://doi.org/10.1093/femsle/fnx134

Pandey A, Soccol CR, Nigam P, Soccol VT (2000) Biotechnological potential of agro-industrial residues. I: sugarcane bagasse. Bioresour Technol 74:69–80. https://doi.org/10.1016/s0960-8524(99)00142-x

Vijayalaxmi S, Jayalakshmi SK, Sreeramulu K (2015) Polyphenols from different agricultural residues: extraction, identification and their antioxidant properties. J Food Sci Technol 52:2761–2769. https://doi.org/10.1007/s13197-014-1295-9

Kachlishvili E, Metreveli E, Elisashvili V (2014) Modulation of Cerrena unicolor laccase and manganese peroxidase production. SpringerPlus 3:463. https://doi.org/10.1186/2193-1801-3-463

Piscitelli A, Giardina P, Lettera V, Pezzella C, Sannia G, Faraco V (2011) Induction and transcriptional regulation of laccases in fungi. Curr Genomics 12:104–112. https://doi.org/10.2174/138920211795564331

Kachlishvili E, Asatiani M, Kobakhidze A, Elisashvili V (2016) Trinitrotoluene and mandarin peels selectively affect lignin-modifying enzyme production in white-rot basidiomycetes. SpringerPlus 5:1–9. https://doi.org/10.1186/s40064-016-1895-0

Ramírez-Montoya LA, Hernández-Montoya V, Montes-Morán MA, Jáuregui-Rincón J, Cervantes FJ (2015) Decolorization of dyes with different molecular properties using free and immobilized laccases from Trametes versicolor. J Mol Liq 212:30–37. https://doi.org/10.1016/j.molliq.2015.08.040

Patel VR, Bhatt NS, B̀bhatt H (2013) Involvement of ligninolytic enzymes of Myceliophthora vellerea HQ871747 in decolorization and complete mineralization of reactive blue 220. Chem Eng J 233: 98–108. https://doi.org/10.1016/j.cej.2013.07.110

Munari FM, Gaio TA, Calloni R, Dillon AJP (2007) Decolorization of textile dyes by enzymatic extract and submerged cultures of Pleurotus sajor-caju. World J Microbiol Biotechnol 24:1383–1392. https://doi.org/10.1007/s11274-007-9621-2

Glazunova O, Trushkin N, Moiseenko K, Filimonov I, Fedorova T (2018) Catalytic efficiency of basidiomycete laccases: redox potential versus substrate-binding pocket structure. Catalysts 8:152. https://doi.org/10.3390/catal8040152

Singh RL, Singh PK, Singh RP (2015) Enzymatic decolorization and degradation of azo dyes – a review. Int Biodeterior Biodegradation 104:21–31. https://doi.org/10.1016/j.ibiod.2015.04.027